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Q9JIF5 (PECR_CAVPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal trans-2-enoyl-CoA reductase

EC=1.3.1.38
Gene names
Name:PECR
OrganismCavia porcellus (Guinea pig)
Taxonomic identifier10141 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity.

Catalytic activity

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH. Ref.1

Pathway

Lipid metabolism; fatty acid biosynthesis.

Subunit structure

Interacts with PEX5, probably required to target it into peroxisomes By similarity.

Subcellular location

Peroxisome Ref.1.

Tissue specificity

Expressed in liver. Ref.1

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Biophysicochemical properties

Kinetic parameters:

KM=11 µM for decenoyl-CoA Ref.1

KM=53 µM for NADPH

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
   Cellular componentPeroxisome
   LigandNADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processfatty acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

peroxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionnucleotide binding

Inferred from electronic annotation. Source: InterPro

trans-2-enoyl-CoA reductase (NADPH) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Peroxisomal trans-2-enoyl-CoA reductase
PRO_0000054739

Regions

Nucleotide binding23 – 4725NADP By similarity
Motif300 – 3023Microbody targeting signal By similarity

Sites

Active site1781Proton acceptor By similarity

Amino acid modifications

Modified residue1781Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JIF5 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9C1430D90D4C07C2

FASTA30232,529
        10         20         30         40         50         60 
MGSWTKCQSC LAPGLLQNRA AIVTGGGTGI GKAIAKELLH LGCNVVIASR KFDRLRAAAE 

        70         80         90        100        110        120 
ELKATLPPSN KAEVTPIQCN IRKEEEVNNL MKSTLALYGK IDFLVNNGGG QFWSSPEHIS 

       130        140        150        160        170        180 
SKGWHAVIET NLTGTFYMCK AAYNSWMKEH GGAIVNIIIL LNGQPFVAHS GAARGGVYNL 

       190        200        210        220        230        240 
TKSLALGWAR SGIRINCVAP GTVYSQTAMD NYGDMGKTLF ADAFQKIPAK RLGVPEEVSS 

       250        260        270        280        290        300 
LVCFLLSPAA SFITGQLVNV DGGQSLYCQN HDIPDHDNWP EGVGDLSTVK KMKESFKQKA 


KL 

« Hide

References

[1]"Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs."
Das A.K., Uhler M.D., Hajra A.K.
J. Biol. Chem. 275:24333-24340(2000) [PubMed: 10811639] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 92-118, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF232010 mRNA. Translation: AAF69799.1.
RefSeqXP_003462124.1. XM_003462076.1.

3D structure databases

ProteinModelPortalQ9JIF5.
SMRQ9JIF5. Positions 8-302.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JIF5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCPOT00000011831; ENSCPOP00000010538; ENSCPOG00000011717.
GeneID100725791.

Phylogenomic databases

eggNOGroNOG16912.
GeneTreeENSGT00600000084005.
HOVERGENHBG105268.
InParanoidQ9JIF5.
OMAFYMCKAX.
OrthoDBEOG415GF8.

Family and domain databases

InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PROSITEPS00061. ADH_SHORT. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePECR_CAVPO
AccessionPrimary (citable) accession number: Q9JIF5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: October 1, 2000
Last modified: December 14, 2011
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families